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Captides: rigid junctions between beta sheets and small molecules
Author(s) -
Kier Brandon L.,
Andersen Niels H.
Publication year - 2014
Publication title -
journal of peptide science
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.475
H-Index - 66
eISSN - 1099-1387
pISSN - 1075-2617
DOI - 10.1002/psc.2657
Subject(s) - beta (programming language) , chemistry , molecule , biophysics , nanotechnology , materials science , computer science , biology , organic chemistry , programming language
An extensive series of covalently linked small molecule–peptide adducts based on a terminally capped‐beta hairpin motif is reported. The constructs can be prepared by standard solid‐phase Fmoc chemistry with one to four peptide chains linked to small molecule hubs bearing carboxylic acid moieties. The key feature of interest is the precise, buried environment of the small molecule, and its rigid orientation relative to one or more short but fully structured peptide chain(s). Most of this study employs a minimalist nine residue ‘captide’, a capped β ‐turn, but we illustrate general applicability to peptides which can terminate in a beta strand. The non‐peptide portion of these adducts can include nearly any molecule bearing one or more carboxylic acid groups. Fold‐dependent rigidity sets this strategy apart from the currently available bioconjugation methods, which typically engender significant flexibility between peptide and tag. Applications to catalyst enhancement, drug design, higher‐order assembly, and FRET calibration rulers are discussed. Copyright © 2014 European Peptide Society and John Wiley & Sons, Ltd.